Relevant bibliographies by topics / Peptide antimicrobiens

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Academic literature on the topic 'Peptide antimicrobiens'

Author: Grafiati
Published: 4 June 2021
Last updated: 5 February 2022

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Journal articles on the topic "Peptide antimicrobiens"

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Browne, Katrina, Sudip Chakraborty, Renxun Chen, Mark DP Willcox, David StClair Black, William R. Walsh, and Naresh Kumar. "A New Era of Antibiotics: The Clinical Potential of Antimicrobial Peptides." International Journal of Molecular Sciences 21, no. 19 (September 24, 2020): 7047. http://dx.doi.org/10.3390/ijms21197047.

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Antimicrobial resistance is a multifaceted crisis, imposing a serious threat to global health. The traditional antibiotic pipeline has been exhausted, prompting research into alternate antimicrobial strategies. Inspired by nature, antimicrobial peptides are rapidly gaining attention for their clinical potential as they present distinct advantages over traditional antibiotics. Antimicrobial peptides are found in all forms of life and demonstrate a pivotal role in the innate immune system. Many antimicrobial peptides are evolutionarily conserved, with limited propensity for resistance. Additionally, chemical modifications to the peptide backbone can be used to improve biological activity and stability and reduce toxicity. This review details the therapeutic potential of peptide-based antimicrobials, as well as the challenges needed to overcome in order for clinical translation. We explore the proposed mechanisms of activity, design of synthetic biomimics, and how this novel class of antimicrobial compound may address the need for effective antibiotics. Finally, we discuss commercially available peptide-based antimicrobials and antimicrobial peptides in clinical trials.
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Schröder, J. M. "Peptides épithéliaux antimicrobiens." Annales de Dermatologie et de Vénéréologie 131, no. 4 (April 2004): 411–16. http://dx.doi.org/10.1016/s0151-9638(04)93629-0.

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Ruijne, Fleur, and Oscar P. Kuipers. "Combinatorial biosynthesis for the generation of new-to-nature peptide antimicrobials." Biochemical Society Transactions 49, no. 1 (January 13, 2021): 203–15. http://dx.doi.org/10.1042/bst20200425.

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Natural peptide products are a valuable source of important therapeutic agents, including antibiotics, antivirals and crop protection agents. Aided by an increased understanding of structure–activity relationships of these complex molecules and the biosynthetic machineries that produce them, it has become possible to re-engineer complete machineries and biosynthetic pathways to create novel products with improved pharmacological properties or modified structures to combat antimicrobial resistance. In this review, we will address the progress that has been made using non-ribosomally produced peptides and ribosomally synthesized and post-translationally modified peptides as scaffolds for designed biosynthetic pathways or combinatorial synthesis for the creation of novel peptide antimicrobials.
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Fleeman, Renee M., Luis A. Macias, Jennifer S. Brodbelt, and Bryan W. Davies. "Defining principles that influence antimicrobial peptide activity against capsulatedKlebsiella pneumoniae." Proceedings of the National Academy of Sciences 117, no. 44 (October 21, 2020): 27620–26. http://dx.doi.org/10.1073/pnas.2007036117.

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The extracellular polysaccharide capsule ofKlebsiella pneumoniaeresists penetration by antimicrobials and protects the bacteria from the innate immune system. Host antimicrobial peptides are inactivated by the capsule as it impedes their penetration to the bacterial membrane. While the capsule sequesters most peptides, a few antimicrobial peptides have been identified that retain activity against encapsulatedK. pneumoniae,suggesting that this bacterial defense can be overcome. However, it is unclear what factors allow peptides to avoid capsule inhibition. To address this, we created a peptide analog with strong antimicrobial activity toward severalK. pneumoniaestrains from a previously inactive peptide. We characterized the effects of these two peptides onK. pneumoniae, along with their physical interactions withK. pneumoniaecapsule. Both peptides disrupted bacterial cell membranes, but only the active peptide displayed this activity against capsulatedK. pneumoniae. Unexpectedly, the active peptide showed no decrease in capsule binding, but did lose secondary structure in a capsule-dependent fashion compared with the inactive parent peptide. We found that these characteristics are associated with capsule-peptide aggregation, leading to disruption of theK. pneumoniaecapsule. Our findings reveal a potential mechanism for disrupting the protective barrier thatK. pneumoniaeuses to avoid the immune system and last-resort antibiotics.
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Schröder, Jens-Michael, and Jürgen Harder. "Peptides antimicrobiens naturels cutanés." médecine/sciences 22, no. 2 (February 2006): 153–57. http://dx.doi.org/10.1051/medsci/2006222153.

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Dong, Na, Chensi Wang, Xinran Li, Yuming Guo, and Xiaoli Li. "Simplified Head-to-Tail Cyclic Polypeptides as Biomaterial-Associated Antimicrobials with Endotoxin Neutralizing and Anti-Inflammatory Capabilities." International Journal of Molecular Sciences 20, no. 23 (November 25, 2019): 5904. http://dx.doi.org/10.3390/ijms20235904.

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The therapeutic application of antimicrobial peptides (AMPs), a potential type of peptide-based biomaterial, is impeded by their poor antimicrobial activity and potential cytotoxicity as a lack of understanding of their structure–activity relationships. In order to comprehensively enhance the antibacterial and clinical application potency of AMPs, a rational approach was applied to design amphiphilic peptides, including head-to-tail cyclic, linear and D-proline antimicrobial peptides using the template (IR)nP(IR)nP (n = 1, 2 and 3). Results showed that these amphiphilic peptides demonstrated antimicrobial activity in a size-dependent manner and that cyclic peptide OIR3, which contained three repeating units (IR)3, had greater antimicrobial potency and cell selectivity than liner peptide IR3, DIR3 with D-Pro and gramicidin S (GS). Surface plasmon resonance and endotoxin neutralization assays indicated that OIR3 had significant endotoxin neutralization capabilities, which suggested that the effects of OIR3 were mediated by binding to lipopolysaccharides (LPS). Using fluorescence spectrometry and electron microscopy, we found that OIR3 strongly promoted membrane disruption and thereby induced cell lysis. In addition, an LPS-induced inflammation assay showed that OIR3 inhibited the pro-inflammatory factor TNF-α in RAW264.7 cells. OIR3 was able to reduce oxazolone-induced skin inflammation in allergic dermatitis mouse model via the inhibition of TNF-α, IL-1β and IL-6 mRNA expression. Collectively, the engineered head-to-tail cyclic peptide OIR3 was considerable potential candidate for use as a clinical therapeutic for the treatment of bacterial infections and skin inflammation.
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Haney, Evan F., Leonard T. Nguyen, David J. Schibli, and Hans J. Vogel. "Design of a novel tryptophan-rich membrane-active antimicrobial peptide from the membrane-proximal region of the HIV glycoprotein, gp41." Beilstein Journal of Organic Chemistry 8 (July 24, 2012): 1172–84. http://dx.doi.org/10.3762/bjoc.8.130.

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A number of physicochemical characteristics have been described which contribute to the biological activity of antimicrobial peptides. This information was used to design a novel antimicrobial peptide sequence by using an intrinsically inactive membrane-associated peptide derived from the HIV glycoprotein, gp41, as a starting scaffold. This peptide corresponds to the tryptophan-rich membrane-proximal region of gp41, which is known to interact at the interfacial region of the viral membrane and adopts a helical structure in the presence of lipids. Three synthetic peptides were designed to increase the net positive charge and amphipathicity of this 19-residue peptide. Ultimately, the peptide with the greatest degree of amphipathicity and largest positive charge proved to be the most potent antimicrobial, and this peptide could be further modified to improve the antimicrobial activity. However, the other two peptides were relatively ineffective antimicrobials and instead proved to be extremely hemolytic. This work demonstrates a novel approach for the design of unexplored antimicrobial peptide sequences but it also reveals that the biological and cytotoxic activities of these polypeptides depend on a number of interrelated factors.
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Kraszewska, Joanna, Michael C. Beckett, Tharappel C. James, and Ursula Bond. "Comparative Analysis of the Antimicrobial Activities of Plant Defensin-Like and Ultrashort Peptides against Food-Spoiling Bacteria." Applied and Environmental Microbiology 82, no. 14 (May 6, 2016): 4288–98. http://dx.doi.org/10.1128/aem.00558-16.

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ABSTRACTAntimicrobial peptides offer potential as novel therapeutics to combat food spoilage and poisoning caused by pathogenic and nonpathogenic bacteria. Our previous studies identified the peptide human beta-defensin 3 (HBD3) as a potent antimicrobial agent against a wide range of beer-spoiling bacteria. Thus, HBD3 is an excellent candidate for development as an additive to prevent food and beverage spoilage. To expand the repertoire of peptides with antimicrobial activity against bacteria associated with food spoilage and/or food poisoning, we carried out anin silicodiscovery pipeline to identify peptides with structure and activity similar to those of HBD3, focusing on peptides of plant origin. Using a standardized assay, we compared the antimicrobial activities of nine defensin-like plant peptides to the activity of HBD3. Only two of the peptides, fabatin-2 and Cp-thionin-2, displayed antimicrobial activity; however, the peptides differed from HBD3 in being sensitive to salt and were thermostable. We also compared the activities of several ultrashort peptides to that of HBD3. One of the peptides, the synthetic tetrapeptide O3TR, displayed biphasic antimicrobial activity but had a narrower host range than HBD3. Finally, to determine if the peptides might act in concert to improve antimicrobial activity, we compared the activities of the peptides in pairwise combinations. The plant defensin-like peptides fabatin-2 and Cp-thionin-2 displayed a synergistic effect with HBD3, while O3TR was antagonistic. Thus, some plant defensin-like peptides are effective antimicrobials and may act in concert with HBD3 to control bacteria associated with food spoilage and food poisoning.IMPORTANCEFood spoilage and food poisoning caused by bacteria can have major health and economic implications for human society. With the rise in resistance to conventional antibiotics, there is a need to identify new antimicrobials to combat these outbreaks in our food supply. Here we screened plant peptide databases to identify peptides that share structural similarity with the human defensin peptide HBD3, which has known antimicrobial activity against food-spoiling bacteria. We show that two of the plant peptides display antimicrobial activity against bacteria associated with food spoilage. When combined with HBD3, the peptides are highly effective. We also analyzed the activity of an easily made ultrashort synthetic peptide, O3TR. We show that this small peptide also displays antimicrobial activity against food-spoiling bacteria but is not as effective as HBD3 or the plant peptides. The plant peptides identified are good candidates for development as natural additives to prevent food spoilage.
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Małuch, Izabela, Oktawian Stachurski, Paulina Kosikowska-Adamus, Marta Makowska, Marta Bauer, Dariusz Wyrzykowski, Aleksandra Hać, et al. "Double-Headed Cationic Lipopeptides: An Emerging Class of Antimicrobials." International Journal of Molecular Sciences 21, no. 23 (November 25, 2020): 8944. http://dx.doi.org/10.3390/ijms21238944.

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Antimicrobial peptides (AMPs) constitute a promising tool in the development of novel therapeutic agents useful in a wide range of bacterial and fungal infections. Among the modifications improving pharmacokinetic and pharmacodynamic characteristics of natural AMPs, an important role is played by lipidation. This study focuses on the newly designed and synthesized lipopeptides containing multiple Lys residues or their shorter homologues with palmitic acid (C16) attached to the side chain of a residue located in the center of the peptide sequence. The approach resulted in the development of lipopeptides representing a model of surfactants with two polar headgroups. The aim of this study is to explain how variations in the length of the peptide chain or the hydrocarbon side chain of an amino acid residue modified with C16, affect biological functions of lipopeptides, their self-assembling propensity, and their mode of action.
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Shao, Changxuan, Weizhong Li, Peng Tan, Anshan Shan, Xiujing Dou, Deying Ma, and Chunyu Liu. "Symmetrical Modification of Minimized Dermaseptins to Extend the Spectrum of Antimicrobials with Endotoxin Neutralization Potency." International Journal of Molecular Sciences 20, no. 6 (March 20, 2019): 1417. http://dx.doi.org/10.3390/ijms20061417.

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Antimicrobial peptides (AMPs) have emerged as a promising class of antimicrobial agents that could potentially address the global antibiotic resistance. Generating mirror-like peptides by minimizing dermaseptin family sequences is an effective strategy for designing AMPs. However, the previous research still had some limitations such as lower effectiveness and a narrow spectrum of antibacterial activity. To further expand and hone this strategy, we designed a series of AMPs consisting of the WXMXW-NH2 motif (X represents V, I, F, and W; M represents KAAAKAAAK). The peptides formed α-helices and displayed broad-spectrum antimicrobial activities against eleven types of clinical bacteria including both Gram-negative and Gram-positive bacteria. The optimized peptide WW exhibited high physical rupture by inducing membrane shrinkage, disruption, and lysis. Moreover, WW effectively neutralized endotoxins and inhibited the inflammatory response while having the highest therapeutic index. In conclusion, these results indicated that the peptide WW has potential as a broad-spectrum antimicrobial agent or preservative for overcoming the risk of multidrug resistance in localized or external therapeutic applications.
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Dissertations / Theses on the topic "Peptide antimicrobiens"

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Cheng, Didier. "Étude comparative des peptides antimicrobiens et des peptides pénétrants." Thesis, Sorbonne université, 2018. http://www.theses.fr/2018SORUS294.

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Les peptides à visée thérapeutique suscitent une attention croissante auprès des industries pharmaceutiques en raison de leur forte activité biologique. Parmi ces peptides, les peptides antimicrobiens (AMP) peuvent éliminer une grande gamme de microorganismes tels que les bactéries et les champignons pathogènes en perturbant leurs membranes tout en ne provoquant qu’une résistance bactérienne limitée contrairement aux antibiotiques couramment utilisés. D’autre part, les peptides vecteurs (CPP) se distinguent par leur capacité à traverser les membranes cellulaires eucaryotes sans les endommager. Cette particularité peut être exploitée pour l’internalisation intracellulaire de molécules bioactives. Malgré leurs différences, les AMP et les CPP sont des peptides membranotropes qui partagent de nombreuses similitudes telles que la taille, la présence d’acides aminés chargés positivement et les structures secondaires qu’ils peuvent adopter, telles que la structure en hélice α. Le projet décrit ici propose de déterminer quels sont les paramètres qui peuvent conférer une activité antimicrobienne ou pénétrante à une séquence peptidique. À cet effet, des séquences inspirées d’un AMP naturel et modifiées par substitution d’acide(s) aminé(s) afin de promouvoir la capacité à pénétrer les membranes eucaryotes ont été établies et synthétisées pour en étudier l’activité antimicrobienne et la pénétration dans les cellules. Les propriétés physico-chimiques de ces peptides (taille, charge globale, hydrophobie …) ont alors modifiés afin d’étudier l’importance de ces paramètres pour chacune des activités
Recently, therapeutic peptides has particularly retained attention of pharmaceutical industries because of their diversified biological activity and their high specificity. Among them, there are noticeably antimicrobial peptides (AMPs), which can straightly kill microorganisms such as pathogenic bacteria and fungi by disrupting prokaryote cell membranes and induce minimal bacterial resistance unlike commonly used antibiotics. Contrastingly, cell-penetrating peptides (CPPs) are distinguished by their ability to cross eukaryote cell membranes without causing any damages, a property that can be used for intracellular drug delivery. Despite their differences, AMPs and CPPs are both membranotropic peptides which are similar in many aspects considering that they might share similar sizes, polycationic charges and secondary structures such as α-helical structure. This project proposes to determine the parameters that might confer AMP versus CPP properties to a peptide sequence. To achieve this purpose, short sequences inspired from a natural AMP were slightly modified by amino acid substitution to promote cell penetration have been designed and synthesized in order to study their antimicrobial activities and uptake potency in mammalian cells. New peptides varying in size, charge and hydrophobicity were obtained. The study demonstrated that antimicrobial and cell-penetration activities can respectively be induced by a small increase in hydrophobicity and global charge from a non-active peptide
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Petit, Vanessa. "Peptides antimicrobiens de procaryotes et d'eucaryotes : des structures aux mécanismes d'action." Paris 6, 2009. http://www.theses.fr/2009PA066291.

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Duquesne, Sophie. "Peptides antimicrobiens des entérobactériesEtude de la voie de maturation et du mécanisme d'import de la microcine J25, peptide antimicrobien inhibiteur de l'ARN polymérase." Phd thesis, Université Pierre et Marie Curie - Paris VI, 2007. http://tel.archives-ouvertes.fr/tel-00193192.

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La microcine J25 (MccJ25) est un peptide antibactérien inhibiteur de l'ARN polymérase, produit par Escherichia coli AY25 selon la voie ribosomique. Sa structure tridimensionnelle en forme de lasso résulte du clivage d'un précurseur, McjA, et de la formation sur le peptide C-terminal résultant, d'une liaison amide Gly1-Glu8. Nous avons d'abord étudié le mode d'import de MccJ25 dans les bactéries et avons montré in vivo et in vitro qu'elle parasite un transporteur du complexe fer/ferrichrome, FhuA. Ainsi, MccJ25 se lie à FhuA avec un Kd de 1.2 µM, pour former un complexe de stœchiométrie 2:1. La boucle en épingle à cheveu béta définie par les résidus Val11-Pro16 de MccJ25 est nécessaire à cette étape de reconnaissance. Dans un second temps, nous avons étudié la biosynthèse de MccJ25. Nous avons montré par inactivation et complémentation de gènes que les deux protéines, McjB et McjC codées par le cluster génétique de la microcine, sont nécessaires au processus de maturation. McjA, McjB et McjC produites en système recombinant ont permis de montrer que McjB et McjC sont capables de catalyser la conversion de McjA (précurseur linéaire inactif) en MccJ25 dotée d'activité antibactérienne et structurée en lasso. L'étude des similarités de séquences de McjB et McjC indique que McjB serait responsable du clivage protéolytique de McjA et McjC de la formation de la liaison Gly1-Glu8.
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Duquesne, Sophie. "Peptides antimicrobiens des entérobactéries : étude de la voie de maturation et du mécanisme d'import de la microcine J25, peptide antimicrobien inhibiteur de l ARN polymérase." Paris 6, 2007. http://www.theses.fr/2007PA066072.

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MccJ25 est un peptide antibactérien dont la structure tridimensionnelle en forme de lasso résulte du clivage de son précurseur McjA, et de la formation d’une liaison Gly1-Glu8 sur le peptide C-terminal résultant. L’étude du mode d’import bactérien de MccJ25 a montré qu’elle parasite un transporteur du complexe fer/ferrichrome, FhuA. MccJ25 se lie à FhuA avec un Kd de 1. 2 µM, pour former un complexe de stœchiométrie 2:1. La région Val11-Pro16 en épingle à cheveu  de MccJ25 est nécessaire à cette interaction. L’étude de la biosynthèse de MccJ25 a montré que les gènes mcjB et mcjC du cluster génétique de MccJ25 sont nécessaires à la production de MccJ25 mature. La production de McjA, McjB et McjC recombinantes a permis de montrer que McjB et McjC sont capables de catalyser la conversion de McjA en MccJ25 structurée en lasso. L’étude des similarités de séquences de McjB et McjC indique que McjB réaliserait le clivage protéolytique de McjA et McjC formerait la liaison Gly1-Glu8.
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Thomas, Xavier. "Peptides antimicrobiens des entérobactéries : la microcine E492 est un peptide-sidérophore qui parasite les voies d'import du fer." Paris 6, 2005. http://www.theses.fr/2005PA066075.

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Blond, Alain. "Les microcines C51 et J25, peptides antimicrobiens d'Entérobactéries : études structurales par RMN et modélisation moléculaire : relations structure/activité." Paris 6, 2002. http://www.theses.fr/2002PA066040.

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Shyam, Radhe. "Cationic amphipathic peptoid oligomers as antimicrobial peptide mimics." Thesis, Université Clermont Auvergne‎ (2017-2020), 2018. http://www.theses.fr/2018CLFAC048/document.

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Les organismes vivants produisent des peptides antimicrobiens (PAMs) pour se protéger contre les microbes. La résistance croissante aux antibiotiques nécessite le développement de nouvelles stratégies thérapeutiques et les PAMs sont des candidats prometteurs pour résoudre ce problème. Ils possèdent une activité à large spectre et leur principal mécanisme d'action par perméation de la membrane engendre peu de phénomènes de résistance. Néanmoins, leur faible biodisponibilité empêche leur utilisation. Certaines limitations peuvent être surmontées en développant des mîmes de PAMs qui conservent leur activité mais avec un potentiel thérapeutique accru. Les peptoïdes (oligomères de N-alkylglycine) structurés en hélice cationique amphiphile sont de bons mimes de PAMs. Les peptoïdes sont plus flexibles que les peptides en raison de l'isomérie cis/trans des amides N,N-disubstitués ; cependant la conformation des amides peut être contrôlée par un choix judicieux des chaînes latérales. Le but de cette thèse est d'étudier l'influence de chaînes latérales(hydrophobes ou cationiques) bloquant la conformation des amides en cis et induisant une structure hélicoïdale de type PolyProline I (PPI) robuste, sur l’activité antibactérienne et la sélectivité de peptoïdes. La conception, la synthèse et l’étude conformationnelle de nouveaux oligomères peptoïdes cationiques portant des chaînes latérales de type tert-butyle et/ou triazolium ont été réalisées. Dans un premier temps, la synthèse en solution d'oligomères à base de tert-butyle a été développée puis une stratégie de synthèse en phase solide a été mise en place pour accéder aux oligomères à base de 1,2,3-triazolium. Ensuite, ces nouveaux oligomères ont été évalués pour leur activité vis à vis d’un panel de bactéries Gram-positive et Gram-négative, leur l'activité antibiofilm et leur sélectivité cellulaire. Enfin, pour visualiser les effets des peptoïdes amphiphiles sur les bactéries, une étude de microscopie a été réalisée
Living organisms produce antimicrobial peptides (AMPs) to protect themselves against microbes.The growing problem of antimicrobial resistance calls for new therapeutic strategies and the natural AMPs have shown ground-breaking potential to address that issue. They show broad-spectrum activity and their main mechanism of action by bacterial cell membrane disruption implies low emergence of resistance which makes them potent candidates for replacing conventional antibiotics. Nevertheless, few hurdles are impeding their use, notably poor bioavailability profile. Some of these limitations can be overcome by developing peptidomimetics of AMPs which exhibit antibacterial activities together with enhanced therapeutic potential. Peptoids (i.e. N-alkyl glycine oligomers) adopting cationic amphipathic helical structures are mostly competent AMP mimetics. From a conformational point of view, peptoids are fundamentally more flexible than peptides primarily due to the cis/trans isomerism of N,N-disubstituted amides but studies in this area have shown that cis amide conformation can be controlled by careful choice of side-chain to set a PolyProline I-type helical structure of peptoids. In this thesis, the genesis of novel amphipathic cationic peptoids carrying cis-directing tert-butyl and/or triazolium-type side-chains and their untapped potential to act against bacteria will be discussed comprehensively. First, the solutionphase synthesis of tert-butyl-based oligomers was developed. Second, novel method of solid-phase submonomer synthesis was optimised to access 1,2,3-triazolium-based oligomers. Then, the synthesised cationic oligomers were evaluated for their antibacterial potential, followed by antibiofilm activity and cell selectivity assays. In the end, to have insights on the mode of action of amphipathic peptoids, microscopy was carried out
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Vanhoye, Damien. "Analyse évolutive, moléculaire et fonctionnelle des peptides antimicrobiens des amphibiens." Paris 6, 2004. http://www.theses.fr/2004PA066326.

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Mutschler, Angela. "Nouveaux concepts de revêtements antimicrobiens à base de peptides naturels et polypeptides appliqués aux dispositifs médicaux." Thesis, Strasbourg, 2017. http://www.theses.fr/2017STRAE025/document.

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De nos jours, la moitié des infections nosocomiales sont liées à la pose de dispositifs médicaux. Dans ce contexte, nous avons développé deux types de revêtements antimicrobiens adaptés au domaine biomédical. Le premier s'appuie sur le greffage d’un peptide comprenant une séquence d’accroche, une séquence antimicrobienne et un site de clivage spécifique d'un pathogène. La séquence antimicrobienne sera alors libérée uniquement en présence du pathogène. Malgré la réussite de l’accroche du peptide, certains paramètres restent encore à optimiser afin d’obtenir un effet antimicrobien. Le deuxième revêtement s’appuie sur la conception d’un film antimicrobien « couche-par-couche » avec l’utilisation de poly(L-arginine) (PAR) et d’acide hyaluronique (HA). L’influence de la taille des chaînes de PAR a été étudiée et seul le film construit à partir de PAR de 30 résidus possède un effet antibactérien. Avec cette PAR, nous avons démontré que HA est le seul polyanion conduisant à des propriétés antibactériennes. Ces propriétés antimicrobiennes sont maintenues lorsque d’autres homopolypeptides cationiques sont associés à HA
Nowadays, about half of hospital-acquired infections are due to medical devices implantation. In this context, we have developed two types of antimicrobial coatings adapted to the biomedical field. The first one is based on peptide composed of an anchoring sequence, an antimicrobial sequence and a pathogen-specific cleavage site and grafted on the substrate. The antimicrobial site will be released only in the presence of the pathogen through the use of the cleavage site. Despite of the success of peptide grafting, some parameters must be optimized in order to obtain an antimicrobial effect. The second antimicrobial coating concept is based on the layer-by-layer technique by using poly(L-arginine) (PAR) and hyaluronic acid (HA). The effect of the size of PAR chains on the antimicrobial character of the coating was investigated and it is proven that only films composed with PAR of 30 residues present an antibacterial effect. Moreover HA is the only polyanion leading to such antimicrobial multilayer. It is also demonstrated that this antimicrobial properties is maintained when other cationic homopolypeptides are used in association with HA in layer-by-layer films
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Chiumento, Steve. "Les bactériocines RumC, une nouvelle famille de peptides antimicrobiens comme alternative aux antibiotiques conventionnels." Thesis, Université Grenoble Alpes (ComUE), 2019. http://www.theses.fr/2019GREAV018/document.

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Les antibiotiques sont des médicaments qui ont changé notre manière d’aborder les infections bactériennes et sont devenus l’un des symboles de la médecine moderne. Cependant leur utilisation massive a conduit à l'émergence de souches bactériennes multirésistantes. Ce problème est sans aucun doute un des grands défis que la médecine actuelle doit relever. Sachant que les bactéries évoluent à un rythme plus rapide que la production de nouveaux antibiotiques, il est urgent de trouver des approches alternatives. Il a été mis en évidence que ces mêmes bactéries sont capables de sécréter différents peptides antimicrobiens, ou bactériocines. Ces macromolécules présentent une grande diversité structurale et sont très efficaces pour combattre un grand nombre de souches pathogènes de façon spécifique. Les bactériocines ont un immense potentiel dans les domaines agroalimentaire et pharmaceutique. Notre projet s’intéresse aux bactériocines RumCs produites par une souche dérivée de Ruminococcus gnavus, une bactérie anaérobie stricte, membre dominant du microbiote intestinal humain. Le travail présenté dans ce manuscrit concerne la mise au point d’un système d’expression et de maturation hétérologue chez E. coli de la bactériocine RumC1. La caractérisation biochimique du peptide RumC1 montre que les bactériocines RumCs appartiennent à la famille des sactipeptides pour laquelle l’étape de biosynthèse fait intervenir une enzyme radical-SAM. Les sactipeptides présentent dans leurs séquences peptidiques un ou plusieurs ponts thioéther entre une cystéine et le carbone alpha d’un acide aminé partenaire. RumC1 renferme 4 ponts thioéther ce qui lui confère une structure originale en double épingle à cheveux. L’activité biologique de RumC1 montre que ce peptide est efficace contre un large spectre de bactéries à Gram positif incluant des pathogènes résistants tels que S.aureus et E. faecalis. Dans ces études nous n’avons pas noté de toxicité significative de RumC1 sur différentes lignées cellulaires humaine ni observé de phénomène de résistance. Les travaux en cours visent notamment à définir le mode d’action de RumC1 et à évaluer l’activité biologique de RumC1 dans un contexte d’infection in vivo chez la souris
Antibiotics are drugs that have changed the way we approach bacterial infections and have become one of the symbols of modern medicine. However, their widespread use has led to the emergence of multiresistant bacterial strains. This problem is undoubtedly one of the major challenges facing today's medicine. Knowing that bacteria evolve at a faster rate than the discovery of new antibiotics, it is urgent to find alternative approaches. It has been shown that these same bacteria are capable of secreting antimicrobial peptides, the bacteriocins. These macromolecules have a high structural diversity and are very effective in combating a large number of pathogenic strains in a specific way. Bacteriocins have immense potential in the agro-food and pharmaceutical sectors. Our project focuses on the bacteriocins RumCs produced by a strain derived from Ruminococcus gnavus, a strict anaerobic bacterium of the human intestinal microbiota. The work presented in this manuscript concerns the development of a heterologous expression and maturation system in E. coli of the bacteriocin RumC1. The biochemical characterization of the RumC1 peptide shows that the RumCs bacteriocins belong to the family of sactipeptides for which the biosynthesis step involves a radical-SAM enzyme. The sactipeptides have in their peptide sequences one or more thioether bridges between a cysteine and the alpha carbon of a partner amino acid. RumC1 contains 4 thioether bridges which gives it an original structure in double hairpin. The biological activity of RumC1 shows that this peptide is effective against a broad spectrum of Gram-positive bacteria including resistant pathogens such as S.aureus and E. faecalis. In these studies, we did not note any significant toxicity of RumC1 on different human cell lines nor observed resistance phenomena. Current work aims to define the mode of action of RumC1 and to evaluate the biological activity of RumC1 in an in vivo context of infection in mice
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Books on the topic "Peptide antimicrobiens"

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Atassi, M. Zouhair. Immunobiology of Proteins and Peptides Vi: "Human Immunodeficiency Virus, Antibody Immunoconjugates, Bacterial Vaccines, And Immunomodulators". Springer, 2012.

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Immunobiology of Proteins and Peptides VI: Human Immunodeficiency Virus, Antibody immunoconjugates, Bacterial Vaccines, Immunomodulators (Advances in Experimental Medicine and Biology). Springer, 1992.

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Book chapters on the topic "Peptide antimicrobiens"

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East, Stephen P. "Actinonin and Analogs: Inhibitors of Bacterial Peptide Deformylase." In Antimicrobials, 287–305. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-662-45786-3_15.

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Carter, Guy T., and Leonard A. McDonald. "Uridyl Peptide Antibiotics: Developments in Biosynthesis and Medicinal Chemistry." In Antimicrobials, 177–91. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-662-45786-3_9.

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Cortes, Jesus. "Lantibiotics and Similar Peptides Produced by and Active on Gram-Positives: Discovery, Development and Perspectives." In Antimicrobials, 141–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-662-45786-3_7.

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Lu, Yi-An, Jin-Long Yang, and James P. Tam. "ε-Peptide Chimeras as Novel Antimicrobials." In Advances in Experimental Medicine and Biology, 393–94. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_171.

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Cama, Jehangir, and Stefano Pagliara. "Microfluidic Single-Cell Phenotyping of the Activity of Peptide-Based Antimicrobials." In Methods in Molecular Biology, 237–53. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0928-6_16.

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Montalban-Lopez, Manuel, Andrius Buivydas, and Oscar P. Kuipers. "Purification of Peptide Antimicrobials and Thioether-Stabilized Molecules Produced In Vivo by Lantibiotic Modification Machineries." In Springer Protocols Handbooks, 95–115. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/8623_2015_122.

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"Host-Defense Peptides and Antimicrobials." In Bioactive Peptides, 313. CRC Press, 2009. http://dx.doi.org/10.1201/9781420061161-p3.

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Najjari, Afef, Hiba Mejri, Marwa Jabbari, Haitham Sghaier, Ameur Cherif, and Hadda-Imene Ouzari. "Halocins, Bacteriocin-Like Antimicrobials Produced by the Archaeal Domain: Occurrence and Phylogenetic Diversity in Halobacteriales." In Extremophilic Microbes and Metabolites - Diversity, Bioprespecting and Biotechnological Applications [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.94765.

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Members of extremely halophilic archaea, currently consisting of more than 56 genera and 216 species, are known to produce their specific bacteriocin-like peptides and proteins called halocins, synthesized by the ribosomal pathway. Halocins are diverse in size, consisting of proteins as large as 35 kDa and peptide “microhalocins” as small as 3.6 kDa. Today, about fifteen halocins have been described and only three genes, halC8, halS8 and halH4, coding C8, S8 and H4 halocins respectively have been identified. In this study, a total of 1858 of complete and nearly complete genome sequences of Halobacteria class members were retrieved from the IMG and Genbank databases and then screened for halocin encoding gene content, based on the BLASTP algorithm. A total of 61 amino acid sequences belonging to three halocins classes (C8, HalH4 and S8) were identified within 15 genera with the abundance of C8 class. Phylogenetic analysis based on amino acids sequences showed a clear segregation of the three halocins classes. Halocin S8 was phylogenetically more close to HalH4. No clear segregation on species and genera levels was observed based on halocin C8 analysiscontrary to HalH4 based analysis. Collectively, these results give an overview on halocins diversity within halophilic archaea which can open new research topics that will shed light on halocins as marker for haloarchaeal phylogentic delineation.
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"Natural Antimicrobials in Food Processing: Bacteriocins, Peptides and Chitooligosaccharides." In Frontiers in Anti-Infective Drug Discovery, edited by Eduardo M. Del Aguila, Laidson P. Gomes, Cyntia S. Freitas, Patricia R. Pereira, and Vânia F. Paschoalin, 55–108. BENTHAM SCIENCE PUBLISHERS, 2017. http://dx.doi.org/10.2174/9781681082912117050005.

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Kaur, Tejinder, and Praveen P. Balgir. "Ancient Pediocin to Innovative Antimicrobial." In Advances in Medical Diagnosis, Treatment, and Care, 183–226. IGI Global, 2021. http://dx.doi.org/10.4018/978-1-7998-0307-2.ch009.

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Multi-drug resistance among patients suffering from infectious diseases has reached such proportions as to render them ineffective. WHO has to put out advisories time and again as to regulate their use. The presently available antibiotics are targeted at inhibiting vital biochemical pathways of pathogens, like nucleotide, protein, or cell wall synthesis in a very specific manner. Antibiotics have been rendered ineffective due to chemical modification, gene mutation, or transport mechanisms employed by pathogens. The novel approach to this problem can be naturally occurring antimicrobial peptides like bacteriocins produced by food grade bacteria. Pediocins produced by pediococcal strains have been found to inhibit a broad spectrum of pathogens by mechanisms that are robust enough to withstand development of resistance. Thus, these pediocins are attractive molecular precursors to develop novel antimicrobials. However, their application as such poses challenges that can be overcome with developing innovative technologies of chemical modifications and delivery strategies.
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Conference papers on the topic "Peptide antimicrobiens"

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Valencia, Yeny Y. P., Gabriel C. A. da Hora, and Thereza A. Soares. "INTERAÇÃO DE AGREGADOS DE POPG NA PRESENÇA DE PEPTIDEO ANTIMICROBIANOS LL 37." In Encontro Anual da biofisica 2019. São Paulo: Editora Blucher, 2019. http://dx.doi.org/10.5151/biofisica2019-23.

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Valencia, Yeny Y. P., Gabriel C. A. da Hora, and Thereza A. Soares. "SIMULAÇÃO COMPUTACIONAL DE AGREGADOS DE POPG NA PRESENÇA DO PEPTÍDEO ANTIMICROBIANO LL37." In Encontro Anual da Biofísica 2018. São Paulo: Editora Blucher, 2018. http://dx.doi.org/10.5151/biofisica2018-06.

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Soares, Thereza A. "SIMULAÇÕES COMPUTACIONAIS DE PEPTIDEOS ANTIMICROBIANOS CATIÔNICOS EM MEMBRANAS BIOLÓGICAS: UMA VISÃO MICROSCÓPICA DO PROCESSO." In Encontro Anual da Biofísica 2018. São Paulo: Editora Blucher, 2018. http://dx.doi.org/10.5151/biofisica2018-40.

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Araujo, Iris de, Júlia Lima, Marcia Aparecida Sperança, Luciano Puzer, Sirlei Daffre, Jose Ricardo Murari Pires, and Fernanda Dias da Silva. "Expressão Recombinante do Peptídeo Antimicrobiano e Quelante de Cobre Microplusina, Contendo Modificações em suas Extremidades Amino- e Carboxi-terminais." In V Simpósio de Bioquímica e Biotecnologia. São Paulo: Editora Edgard Blücher, 2015. http://dx.doi.org/10.5151/biochem-vsimbbtec-21974.

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SILVA JUNIOR, A. G., I. A. M. FRIAS, S. R. SÁ, R. G. LIMA-NETO, O. L. FRANCO, M. D. L. OLIVIERA, and C. A. S. ANDRADE. "BIOSSENSOR PARA DETECÇÃO DE STAPHYLOCOCCUS AUREUS BASEADO EM PEPTÍDEO ANTIMICROBIANO MASTOPARANO-L/MO E NANOESTRUTURAS NÚCLEO-CASCA DE Fe3O4@Au." In ANAIS DO 5º ENCONTRO BRASILEIRO PARA INOVAçãO TERAPêUTICA. Galoa, 2017. http://dx.doi.org/10.17648/ebit-2017-85689.

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Waz, Natalha Tedeschi, Bárbara Milani Froes, and Michelle Darrieux. "PAPEL DA CÁPSULA POLISSACARÍDICA E DA PROTEÍNA PspA NA AÇÃO MICROBICIDA DA INDOLICIDINA SOBRE Streptococcus pneumoniae." In I Congresso Brasileiro de Biotecnologia On-line. Revista Multidisciplinar de Educação e Meio Ambiente, 2021. http://dx.doi.org/10.51189/rema/1098.

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Introdução: Streptococcus pneumoniae (pneumococo) é uma bactéria responsável por elevada mortalidade no mundo todo. É um patógeno Gram-positivo extracelular recoberto por uma cápsula polissacarídica. A cápsula confere proteção contra a fagocitose pelo sistema imune, além de influenciar diferentes aspectos da patogênese bacteriana, como adesão e deposição de moléculas do sistema complemento. Devido à sua elevada imunogenicidade, os polissacarídeos capsulares constituem a base das formulações vacinais atualmente disponíveis contra o pneumococo. As cápsulas apresentam elevada variabilidade, permitindo a classificação da bactéria em 96 sorotipos. Os peptídeos antimicrobianos (AMPs) representam uma das primeiras linhas de defesa imune, através da capacidade de promover a lise de diversos patógenos. A indolicidina, um peptídeo catiônico produzido por neutrófilos ativados, apresenta ação bactericida contra o pneumococo. Nosso grupo demonstrou que a presença da proteína PspA – um importante candidato vacinal – na superfície da bactéria apresenta efeito protetor contra a lise por indolicidina. No entanto, a influência de outros fatores de virulência, como cápsula polissacarídica, não foram investigados. Objetivo: O presente estudo tem como objetivo avaliar o papel da cápsula polissacarídica na proteção da bactéria contra a ação lítica da indolicidina. Material e métodos: Inicialmente foi avaliada a sensibilidade à indolicidina de pneumococos de quatro sorotipos capsulares diferentes. Em seguida, foi analisada a resistência à indolicidina em pneumococos selvagens versus mutantes isogênicos sem cápsula. Resultados: Os dados obtidos no primeiro ano de projeto indicam que diferentes sorotipos de pneumococo apresentam variação na resistência à indolicidina; os isolados 245/00 (sorotipo 14) e A66.1 (sorotipo 3) foram mais sensíveis quando comparados à D39 (sorotipo 2). A presença da cápsula também parece influenciar a ação lítica da indolicidina; a bactéria mutante se mostrou mais sensível ao AMP quando comparada à bactéria encapsulada. Conclusão e perspectivas: Os dados obtidos até o momento sugerem que a cápsula desempenha um papel protetor contra a ação da indolicidina e que variações na composição da mesma podem afetar a resistência bacteriana ao peptídeo. Novos ensaios utilizando-se pneumococos de diferentes sorotipos irão confirmar a influência da composição da cápsula na ação da indolicidina, enquanto a comparação de pneumococos selvagens e mutantes sem cápsula com diferentes backgrounds genéticos elucidará o efeito desta estrutura na proteção da bactéria contra este AMP.
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